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Q9UL25

- RAB21_HUMAN

UniProt

Q9UL25 - RAB21_HUMAN

Protein

Ras-related protein Rab-21

Gene

RAB21

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general. As a result, may regulate cell adhesion and migration By similarity. During the mitosis of adherent cells, controls the endosomal trafficking of integrins which is required for the successful completion of cytokinesis.By similarity1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 349GTP
    Nucleotide bindingi74 – 785GTPBy similarity
    Nucleotide bindingi132 – 1354GTP
    Nucleotide bindingi162 – 1643GTP

    GO - Molecular functioni

    1. GDP binding Source: UniProtKB
    2. GTPase activity Source: UniProtKB
    3. GTP binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. GTP catabolic process Source: GOC
    2. protein transport Source: UniProtKB-KW
    3. small GTPase mediated signal transduction Source: InterPro

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.6.5.2. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Rab-21
    Gene namesi
    Name:RAB21
    Synonyms:KIAA0118
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18263. RAB21.

    Subcellular locationi

    Endoplasmic reticulum membrane By similarity; Lipid-anchor By similarity. Golgi apparatus membrane. Early endosome membrane. Cytoplasmic vesicle membrane. Cleavage furrow
    Note: In nonpolarized epithelial Caco-2 cells, found in the endoplasmic reticulum; in polarized cells, observed in vesicles in the apical cytoplasm. During mitosis, in mid-telophase, localized in the ingressing cleavage furrow. In late telophase, detected at the opposite poles of the daughter cells, in vesicles at the base of lamellipodia formed by the separating daughter cells.

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB-SubCell
    2. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    3. early endosome membrane Source: UniProtKB-SubCell
    4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    5. endosome Source: LIFEdb
    6. extracellular vesicular exosome Source: UniProt
    7. Golgi membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi33 – 331T → N: Defects in GTP-binding. 1 Publication
    Mutagenesisi78 – 781Q → L: Defects in GTP hydrolysis. 1 Publication

    Organism-specific databases

    PharmGKBiPA34111.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 222221Ras-related protein Rab-21PRO_0000121205Add
    BLAST
    Propeptidei223 – 2253Removed in mature formSequence AnalysisPRO_0000370768

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Lipidationi221 – 2211S-geranylgeranyl cysteineBy similarity
    Modified residuei222 – 2221Cysteine methyl esterSequence Analysis
    Lipidationi222 – 2221S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiQ9UL25.
    PaxDbiQ9UL25.
    PeptideAtlasiQ9UL25.
    PRIDEiQ9UL25.

    PTM databases

    PhosphoSiteiQ9UL25.

    Expressioni

    Tissue specificityi

    Widely expressed. In jejunal tissue, predominantly expressed in the apical region of the epithelial cell layer of the villi, weak expression, if any, in the crypt epithelium. Capillary endothelium and some cell types in the lamina propria also show expression.1 Publication

    Gene expression databases

    ArrayExpressiQ9UL25.
    BgeeiQ9UL25.
    CleanExiHS_RAB21.
    GenevestigatoriQ9UL25.

    Organism-specific databases

    HPAiCAB037048.
    HPA016988.

    Interactioni

    Subunit structurei

    Interacts with the cytoplasmic tail of integrins ITGA1, ITGA2, ITGA5, ITGA6, ITGA11 and ITGB1 By similarity. Interacts with RABGEF1 (via VPS9 domain).By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APPL1Q9UKG110EBI-1056039,EBI-741243

    Protein-protein interaction databases

    BioGridi116653. 6 interactions.
    DIPiDIP-29349N.
    IntActiQ9UL25. 5 interactions.
    MINTiMINT-3081967.
    STRINGi9606.ENSP00000261263.

    Structurei

    Secondary structure

    1
    225
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 258
    Helixi28 – 303
    Helixi32 – 4110
    Beta strandi46 – 483
    Beta strandi55 – 6511
    Beta strandi67 – 748
    Helixi79 – 846
    Helixi85 – 895
    Beta strandi93 – 1008
    Helixi104 – 12118
    Helixi122 – 1243
    Beta strandi125 – 1328
    Helixi134 – 1396
    Helixi144 – 15310
    Beta strandi157 – 1626
    Turni163 – 1664
    Helixi169 – 18113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YZTX-ray2.05A/B16-183[»]
    1YZUX-ray2.50A/B16-183[»]
    1Z08X-ray1.80A/B/C/D16-183[»]
    1Z0IX-ray2.33A16-183[»]
    2OT3X-ray2.10B16-183[»]
    ProteinModelPortaliQ9UL25.
    SMRiQ9UL25. Positions 17-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UL25.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi48 – 569Effector regionBy similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233968.
    HOVERGENiHBG009351.
    InParanoidiQ9UL25.
    KOiK07890.
    OMAiSHFFASA.
    OrthoDBiEOG7RZ5QX.
    PhylomeDBiQ9UL25.
    TreeFamiTF300199.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00175. RAB. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51419. RAB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UL25-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAGGGGGG AAAAGRAYSF KVVLLGEGCV GKTSLVLRYC ENKFNDKHIT    50
    TLQASFLTKK LNIGGKRVNL AIWDTAGQER FHALGPIYYR DSNGAILVYD 100
    ITDEDSFQKV KNWVKELRKM LGNEICLCIV GNKIDLEKER HVSIQEAESY 150
    AESVGAKHYH TSAKQNKGIE ELFLDLCKRM IETAQVDERA KGNGSSQPGT 200
    ARRGVQIIDD EPQAQTSGGG CCSSG 225
    Length:225
    Mass (Da):24,348
    Last modified:January 23, 2007 - v3
    Checksum:i73CA2C127F0CBFD6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091035 mRNA. Translation: AAF00048.1.
    BC021901 mRNA. Translation: AAH21901.1.
    BC092475 mRNA. Translation: AAH92475.1.
    D42087 mRNA. Translation: BAA07682.1.
    CCDSiCCDS9003.1.
    RefSeqiNP_055814.1. NM_014999.2.
    UniGeneiHs.524590.

    Genome annotation databases

    EnsembliENST00000261263; ENSP00000261263; ENSG00000080371.
    GeneIDi23011.
    KEGGihsa:23011.
    UCSCiuc001swt.3. human.

    Polymorphism databases

    DMDMi13633613.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091035 mRNA. Translation: AAF00048.1 .
    BC021901 mRNA. Translation: AAH21901.1 .
    BC092475 mRNA. Translation: AAH92475.1 .
    D42087 mRNA. Translation: BAA07682.1 .
    CCDSi CCDS9003.1.
    RefSeqi NP_055814.1. NM_014999.2.
    UniGenei Hs.524590.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YZT X-ray 2.05 A/B 16-183 [» ]
    1YZU X-ray 2.50 A/B 16-183 [» ]
    1Z08 X-ray 1.80 A/B/C/D 16-183 [» ]
    1Z0I X-ray 2.33 A 16-183 [» ]
    2OT3 X-ray 2.10 B 16-183 [» ]
    ProteinModelPortali Q9UL25.
    SMRi Q9UL25. Positions 17-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116653. 6 interactions.
    DIPi DIP-29349N.
    IntActi Q9UL25. 5 interactions.
    MINTi MINT-3081967.
    STRINGi 9606.ENSP00000261263.

    PTM databases

    PhosphoSitei Q9UL25.

    Polymorphism databases

    DMDMi 13633613.

    Proteomic databases

    MaxQBi Q9UL25.
    PaxDbi Q9UL25.
    PeptideAtlasi Q9UL25.
    PRIDEi Q9UL25.

    Protocols and materials databases

    DNASUi 23011.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261263 ; ENSP00000261263 ; ENSG00000080371 .
    GeneIDi 23011.
    KEGGi hsa:23011.
    UCSCi uc001swt.3. human.

    Organism-specific databases

    CTDi 23011.
    GeneCardsi GC12P072100.
    HGNCi HGNC:18263. RAB21.
    HPAi CAB037048.
    HPA016988.
    MIMi 612398. gene.
    neXtProti NX_Q9UL25.
    PharmGKBi PA34111.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233968.
    HOVERGENi HBG009351.
    InParanoidi Q9UL25.
    KOi K07890.
    OMAi SHFFASA.
    OrthoDBi EOG7RZ5QX.
    PhylomeDBi Q9UL25.
    TreeFami TF300199.

    Enzyme and pathway databases

    BRENDAi 3.6.5.2. 2681.

    Miscellaneous databases

    ChiTaRSi RAB21. human.
    EvolutionaryTracei Q9UL25.
    GeneWikii RAB21.
    GenomeRNAii 23011.
    NextBioi 43928.
    PROi Q9UL25.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UL25.
    Bgeei Q9UL25.
    CleanExi HS_RAB21.
    Genevestigatori Q9UL25.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of Rab small GTPases in epithelial Caco-2 cells: Rab21 is an apically located GTP-binding protein in polarised intestinal epithelial cells."
      Opdam F.J.M., Kamps G., Croes H., van Bokhoven H., Ginsel L.A., Fransen J.A.M.
      Eur. J. Cell Biol. 79:308-316(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Colon carcinoma.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lymph and Placenta.
    3. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-16; 48-59; 91-109 AND 141-157, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    4. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
      DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-225.
      Tissue: Bone marrow.
    5. Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF THR-33 AND GLN-78.
    6. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
      Eathiraj S., Pan X., Ritacco C., Lambright D.G.
      Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 16-183 IN COMPLEX WITH GTP ANALOG AND GDP.
    11. "Structural basis for Rab GTPase activation by VPS9 domain exchange factors."
      Delprato A., Lambright D.G.
      Nat. Struct. Mol. Biol. 14:406-412(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-183 IN COMPLEX WITH RABGEF1.

    Entry informationi

    Entry nameiRAB21_HUMAN
    AccessioniPrimary (citable) accession number: Q9UL25
    Secondary accession number(s): Q14466, Q569H3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 140 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3